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Volumn 414, Issue 1, 2011, Pages 79-83

Crocetin inhibits beta-amyloid fibrillization and stabilizes beta-amyloid oligomers

Author keywords

Beta amyloid; Crocetin; Fibril; Oligomer; Protein aggregation

Indexed keywords

AMYLOID BETA PROTEIN; CROCETIN; OLIGOMER;

EID: 80054071097     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.09.025     Document Type: Article
Times cited : (41)

References (39)
  • 1
    • 77649202326 scopus 로고    scopus 로고
    • Protein aggregation diseases: pathogenicity and therapeutic perspectives
    • Aguzzi A., O'Connor T. Protein aggregation diseases: pathogenicity and therapeutic perspectives. Nat. Rev. Drug Discov. 2010, 9:237-248.
    • (2010) Nat. Rev. Drug Discov. , vol.9 , pp. 237-248
    • Aguzzi, A.1    O'Connor, T.2
  • 2
    • 77951776829 scopus 로고    scopus 로고
    • Alzheimer's disease: strategies for disease modification
    • Citron M. Alzheimer's disease: strategies for disease modification. Nat. Rev. Drug Discov. 2010, 9:387-398.
    • (2010) Nat. Rev. Drug Discov. , vol.9 , pp. 387-398
    • Citron, M.1
  • 6
    • 0033932761 scopus 로고    scopus 로고
    • Intravenous crocetinate prolongs survival in a rat model of lethal hypoxemia
    • Singer M., Stidwill R.P., Nathan A., Gainer J.L. Intravenous crocetinate prolongs survival in a rat model of lethal hypoxemia. Crit. Care Med. 2000, 28:1968-1972.
    • (2000) Crit. Care Med. , vol.28 , pp. 1968-1972
    • Singer, M.1    Stidwill, R.P.2    Nathan, A.3    Gainer, J.L.4
  • 7
    • 34247890129 scopus 로고    scopus 로고
    • Crocetin, dimethylcrocetin, and safranal bind human serum albumin: stability and antioxidative properties
    • Kanakis C.D., Tarantilis P.A., Tajmir-Riahi H.A., Polissiou M.G. Crocetin, dimethylcrocetin, and safranal bind human serum albumin: stability and antioxidative properties. J. Agric. Food Chem. 2007, 55:970-977.
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 970-977
    • Kanakis, C.D.1    Tarantilis, P.A.2    Tajmir-Riahi, H.A.3    Polissiou, M.G.4
  • 8
    • 0016852683 scopus 로고
    • The use of crocetin in experimental atherosclerosis
    • Gainer J.L., Jones J.R. The use of crocetin in experimental atherosclerosis. Experientia 1975, 31:548-549.
    • (1975) Experientia , vol.31 , pp. 548-549
    • Gainer, J.L.1    Jones, J.R.2
  • 10
    • 25444434647 scopus 로고    scopus 로고
    • Orally administered crocetin and crocins are absorbed into blood plasma as crocetin and its glucuronide conjugates in mice
    • Asai A., Nakano T., Takahashi M., Nagao A. Orally administered crocetin and crocins are absorbed into blood plasma as crocetin and its glucuronide conjugates in mice. J. Agric. Food Chem. 2005, 53:7302-7306.
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 7302-7306
    • Asai, A.1    Nakano, T.2    Takahashi, M.3    Nagao, A.4
  • 11
  • 12
    • 7644225312 scopus 로고    scopus 로고
    • RAGE (yin) versus LRP (yang) balance regulates alzheimer amyloid beta-peptide clearance through transport across the blood-brain barrier
    • Deane R., Wu Z., Zlokovic B.V. RAGE (yin) versus LRP (yang) balance regulates alzheimer amyloid beta-peptide clearance through transport across the blood-brain barrier. Stroke 2004, 35:2628-2631.
    • (2004) Stroke , vol.35 , pp. 2628-2631
    • Deane, R.1    Wu, Z.2    Zlokovic, B.V.3
  • 13
    • 78651245383 scopus 로고    scopus 로고
    • Stoichiometry and affinity of the human serum albumin-Alzheimer's Abeta peptide interactions
    • Milojevic J., Melacini G. Stoichiometry and affinity of the human serum albumin-Alzheimer's Abeta peptide interactions. Biophys. J. 2011, 100:183-192.
    • (2011) Biophys. J. , vol.100 , pp. 183-192
    • Milojevic, J.1    Melacini, G.2
  • 14
    • 78449245429 scopus 로고    scopus 로고
    • A strategy for designing a peptide probe for detection of beta-amyloid oligomers
    • Hu Y., Su B., Kim C.S., Hernandez M., Rostagno A., Ghiso J., Kim J.R. A strategy for designing a peptide probe for detection of beta-amyloid oligomers. Chembiochem 2010, 11:2409-2418.
    • (2010) Chembiochem , vol.11 , pp. 2409-2418
    • Hu, Y.1    Su, B.2    Kim, C.S.3    Hernandez, M.4    Rostagno, A.5    Ghiso, J.6    Kim, J.R.7
  • 15
    • 33749535361 scopus 로고    scopus 로고
    • Preparation of amyloid beta-protein for structural and functional studies
    • Teplow D.B. Preparation of amyloid beta-protein for structural and functional studies. Methods Enzymol. 2006, 413:20-33.
    • (2006) Methods Enzymol. , vol.413 , pp. 20-33
    • Teplow, D.B.1
  • 16
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of beta-sheet amyloid fibril structures with thioflavin T
    • LeVine H. Quantification of beta-sheet amyloid fibril structures with thioflavin T. Methods Enzymol. 1999, 309:274-284.
    • (1999) Methods Enzymol. , vol.309 , pp. 274-284
    • LeVine, H.1
  • 17
    • 0018374688 scopus 로고
    • A graphical correction procedure for inner filter effect in fluorescence quenching titrations
    • Mertens M.L., Kagi J.H. A graphical correction procedure for inner filter effect in fluorescence quenching titrations. Anal. Biochem. 1979, 96:448-455.
    • (1979) Anal. Biochem. , vol.96 , pp. 448-455
    • Mertens, M.L.1    Kagi, J.H.2
  • 18
    • 37049080392 scopus 로고
    • Experimental correction for the inner-filter effect in fluorescence spectra
    • Kubista M., Sjoback R., Eriksson S., Albinsson B. Experimental correction for the inner-filter effect in fluorescence spectra. Analyst 1994, 119:417-419.
    • (1994) Analyst , vol.119 , pp. 417-419
    • Kubista, M.1    Sjoback, R.2    Eriksson, S.3    Albinsson, B.4
  • 19
    • 0017996882 scopus 로고
    • Corrections for inner-filter effects in fluorescence quenching measurements via right-angle and front-surface illumination
    • Leese R.A., Wehry E.L. Corrections for inner-filter effects in fluorescence quenching measurements via right-angle and front-surface illumination. Anal. Chem. 1978, 50:1193-1197.
    • (1978) Anal. Chem. , vol.50 , pp. 1193-1197
    • Leese, R.A.1    Wehry, E.L.2
  • 20
    • 35148888521 scopus 로고    scopus 로고
    • Rapid determination of enzyme kinetics from fluorescence: overcoming the inner filter effect
    • Palmier M.O., Van Doren S.R. Rapid determination of enzyme kinetics from fluorescence: overcoming the inner filter effect. Anal. Biochem. 2007, 371:43-51.
    • (2007) Anal. Biochem. , vol.371 , pp. 43-51
    • Palmier, M.O.1    Van Doren, S.R.2
  • 21
    • 79955382682 scopus 로고    scopus 로고
    • Non-esterified fatty acids generate distinct low-molecular weight amyloid-beta (Abeta42) oligomers along pathway different from fibril formation
    • Kumar A., Bullard R.L., Patel P., Paslay L.C., Singh D., Bienkiewicz E.A., Morgan S.E., Rangachari V. Non-esterified fatty acids generate distinct low-molecular weight amyloid-beta (Abeta42) oligomers along pathway different from fibril formation. PLoS One 2011, 6:e18759.
    • (2011) PLoS One , vol.6
    • Kumar, A.1    Bullard, R.L.2    Patel, P.3    Paslay, L.C.4    Singh, D.5    Bienkiewicz, E.A.6    Morgan, S.E.7    Rangachari, V.8
  • 24
    • 34249860495 scopus 로고    scopus 로고
    • Small molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct
    • Necula M., Kayed R., Milton S., Glabe C.G. Small molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct. J. Biol. Chem. 2007, 282:10311-10324.
    • (2007) J. Biol. Chem. , vol.282 , pp. 10311-10324
    • Necula, M.1    Kayed, R.2    Milton, S.3    Glabe, C.G.4
  • 25
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F., Dobson C.M. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 2006, 75:333-366.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 26
    • 33845978790 scopus 로고    scopus 로고
    • Insight into the structure of amyloid fibrils from the analysis of globular proteins
    • Trovato A., Chiti F., Maritan A., Seno F. Insight into the structure of amyloid fibrils from the analysis of globular proteins. PLoS Comput. Biol. 2006, 2:e170.
    • (2006) PLoS Comput. Biol. , vol.2
    • Trovato, A.1    Chiti, F.2    Maritan, A.3    Seno, F.4
  • 28
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
    • Fernandez-Escamilla A.M., Rousseau F., Schymkowitz J., Serrano L. Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nat. Biotechnol. 2004, 22:1302-1306.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1302-1306
    • Fernandez-Escamilla, A.M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 29
    • 0031587286 scopus 로고    scopus 로고
    • Acetylcholinesterase promotes the aggregation of amyloid-beta-peptide fragments by forming a complex with the growing fibrils
    • Alvarez A., Opazo C., Alarcon R., Garrido J., Inestrosa N.C. Acetylcholinesterase promotes the aggregation of amyloid-beta-peptide fragments by forming a complex with the growing fibrils. J. Mol. Biol. 1997, 272:348-361.
    • (1997) J. Mol. Biol. , vol.272 , pp. 348-361
    • Alvarez, A.1    Opazo, C.2    Alarcon, R.3    Garrido, J.4    Inestrosa, N.C.5
  • 31
    • 77954892793 scopus 로고    scopus 로고
    • Polymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape
    • Miller Y., Ma B., Nussinov R. Polymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape. Chem. Rev. 2010, 110:4820-4838.
    • (2010) Chem. Rev. , vol.110 , pp. 4820-4838
    • Miller, Y.1    Ma, B.2    Nussinov, R.3
  • 33
    • 33846565857 scopus 로고    scopus 로고
    • Early kinetics of amyloid fibril formation reveals conformational reorganisation of initial aggregates
    • Cerda-Costa N., Esteras-Chopo A., Aviles F.X., Serrano L., Villegas V. Early kinetics of amyloid fibril formation reveals conformational reorganisation of initial aggregates. J. Mol. Biol. 2007, 366:1351-1363.
    • (2007) J. Mol. Biol. , vol.366 , pp. 1351-1363
    • Cerda-Costa, N.1    Esteras-Chopo, A.2    Aviles, F.X.3    Serrano, L.4    Villegas, V.5
  • 36
    • 79953198908 scopus 로고    scopus 로고
    • Saffron extract and trans-crocetin inhibit glutamatergic synaptic transmission in rat cortical brain slices
    • Berger F., Hensel A., Nieber K. Saffron extract and trans-crocetin inhibit glutamatergic synaptic transmission in rat cortical brain slices. Neuroscience 2011, 180:238-247.
    • (2011) Neuroscience , vol.180 , pp. 238-247
    • Berger, F.1    Hensel, A.2    Nieber, K.3
  • 37
    • 57649148788 scopus 로고    scopus 로고
    • Structural classification of toxic amyloid oligomers
    • Glabe C.G. Structural classification of toxic amyloid oligomers. J. Biol. Chem. 2008, 283:29639-29643.
    • (2008) J. Biol. Chem. , vol.283 , pp. 29639-29643
    • Glabe, C.G.1
  • 39
    • 80053595082 scopus 로고    scopus 로고
    • Protein engineering to stabilize soluble amyloid beta-protein aggregates for structural and functional studies
    • Hard T. Protein engineering to stabilize soluble amyloid beta-protein aggregates for structural and functional studies. FEBS J. 2011, 10.1111/j.1742-4658.2011.08295.x.
    • (2011) FEBS J.
    • Hard, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.